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Database: UniProt
Entry: Q4CPV7_TRYCC
LinkDB: Q4CPV7_TRYCC
Original site: Q4CPV7_TRYCC 
ID   Q4CPV7_TRYCC            Unreviewed;       477 AA.
AC   Q4CPV7;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=protein-synthesizing GTPase {ECO:0000256|ARBA:ARBA00011986};
DE            EC=3.6.5.3 {ECO:0000256|ARBA:ARBA00011986};
GN   ORFNames=Tc00.1047053503819.30 {ECO:0000313|EMBL:EAN82311.1},
GN   Tc00.1047053510359.310 {ECO:0000313|EMBL:EAN99902.1};
OS   Trypanosoma cruzi (strain CL Brener).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=353153 {ECO:0000313|Proteomes:UP000002296};
RN   [1] {ECO:0000313|EMBL:EAN82311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CL Brener {ECO:0000313|EMBL:EAN82311.1};
RX   PubMed=16020724; DOI=10.1126/science.1112181;
RA   El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA   Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA   Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA   Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA   Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA   Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA   Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA   Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA   Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT   "Comparative genomics of trypanosomatid parasitic protozoa.";
RL   Science 309:404-409(2005).
RN   [2] {ECO:0000313|EMBL:EAN82311.1, ECO:0000313|Proteomes:UP000002296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL Brener {ECO:0000313|EMBL:EAN82311.1,
RC   ECO:0000313|Proteomes:UP000002296};
RX   PubMed=16020725; DOI=10.1126/science.1112631;
RA   El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA   Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA   Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA   Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA   Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA   da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA   Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA   Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA   Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA   Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA   Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA   Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA   Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA   Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA   Andersson B.;
RT   "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT   disease.";
RL   Science 309:409-415(2005).
RN   [3] {ECO:0000313|EMBL:EAN82311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CL Brener {ECO:0000313|EMBL:EAN82311.1};
RA   El-Sayed N., Bartholomeu D., Haas B.;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0007829|PDB:7ASE}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.33 ANGSTROMS).
RX   PubMed=33357443; DOI=10.1016/j.celrep.2020.108534;
RA   Bochler A., Querido J.B., Prilepskaja T., Soufari H., Simonetti A.,
RA   Del Cistia M.L., Kuhn L., Ribeiro A.R., Valasek L.S., Hashem Y.;
RT   "Structural Differences in Translation Initiation between Pathogenic
RT   Trypanosomatids and Their Mammalian Hosts.";
RL   Cell Rep. 33:108534-108534(2020).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001874};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAN82311.1}.
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DR   EMBL; AAHK01002572; EAN82311.1; -; Genomic_DNA.
DR   EMBL; AAHK01000007; EAN99902.1; -; Genomic_DNA.
DR   RefSeq; XP_804162.1; XM_799069.1.
DR   RefSeq; XP_821753.1; XM_816660.1.
DR   PDB; 7ASE; EM; 3.33 A; 5=1-477.
DR   AlphaFoldDB; Q4CPV7; -.
DR   EMDB; EMD-11893; -.
DR   SMR; Q4CPV7; -.
DR   STRING; 353153.Q4CPV7; -.
DR   PaxDb; 353153-Q4CPV7; -.
DR   EnsemblProtists; EAN82311; EAN82311; Tc00.1047053503819.30.
DR   EnsemblProtists; EAN99902; EAN99902; Tc00.1047053510359.310.
DR   GeneID; 3533520; -.
DR   GeneID; 3554746; -.
DR   KEGG; tcr:503819.30; -.
DR   KEGG; tcr:510359.310; -.
DR   eggNOG; KOG0466; Eukaryota.
DR   InParanoid; Q4CPV7; -.
DR   OrthoDB; 1512042at2759; -.
DR   Proteomes; UP000002296; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   CDD; cd01888; eIF2_gamma; 1.
DR   CDD; cd03688; eIF2_gamma_II; 1.
DR   CDD; cd15490; eIF2_gamma_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR015256; eIF2g_C.
DR   InterPro; IPR044127; eIF2g_dom_2.
DR   InterPro; IPR044128; eIF2g_GTP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   PANTHER; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR42854:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED; 1.
DR   Pfam; PF09173; eIF2_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:7ASE};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000313|EMBL:EAN82311.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002296}.
FT   DOMAIN          50..256
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   477 AA;  52580 MW;  3F2F194899D55802 CRC64;
     MDENDIADFT MDENTFVTNE QNERGLATQD INALNLDKIN AETFEVMSRQ ATVNIGTIGH
     VAHGKSTVVK ALSGVKTQKY HREAVMNITI HLGYANAKVF KCDKCELPAA FHAFPSSQPD
     KTDCPTCGSP LTLKRHFSFV DCPGHDVLMA TMLNGAAIMD AALLLIAANE PFPQPQTLEH
     LKAVEIMRLA NLVILQNKID LVGEVHAQDQ YHKIRNYIDS TIGSNIPIIP ISAQLKRNID
     YLLEYLCHIP LPTRQLNCPA HMTVVRSFDI NKPGEVDIEN LRGGVAGGTV TRGIIRVNQV
     LEIRPGQVHA QTGGTFSCTP LRTRALTLKA EDNSLQYAVP GGLIAVGTTL DPTLTRQDKM
     VGHMIADEGS LPEVYAEIEV QYFLFEEMVG RSKQRDRNAK RVQKLNLQET LQINVGTLTA
     GATVVNITKN PDIAKLTLVT PVCCTLDEHI AISRLVEKNF RLIGWGIIRR GVPVKLN
//
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